GroEL

HSPD1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4PJ1
Identifiers
Aliases	HSPD1, CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13, heat shock protein family D (Hsp60) member 1
External IDs	OMIM: 118190 MGI: 96242 HomoloGene: 1626 GeneCards: HSPD1
Gene location (Human)
Chr.	Chromosome 2 (human)
End	197,516,737 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	55,127,402 bp
RNA expression pattern
	Top expressed in
	right adrenal gland; ; left adrenal gland; ; body of pancreas; ; ganglionic eminence; ; rectum; ; right lobe of liver; ; appendix; ; anterior pituitary; ; smooth muscle tissue; ; islet of Langerhans;
	Top expressed in
	ovary; ; adrenal gland; ; proximal tubule; ; yolk sac; ; kidney; ; placenta; ; uterus; ; heart; ; intestine; ; neural tube;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; chaperone binding; p53 binding; single-stranded DNA binding; ATPase activity; protein binding; double-stranded RNA binding; DNA replication origin binding; ATP binding; ubiquitin protein ligase binding; protein folding chaperone activity; unfolded protein binding; RNA binding; hydrolase activity; high-density lipoprotein particle binding; enzyme binding; apolipoprotein binding; apolipoprotein A-I binding; lipopolysaccharide binding; isomerase activity;
Cellular component	cytoplasm; cyclin-dependent protein kinase activating kinase holoenzyme complex; lipopolysaccharide receptor complex; early endosome; mitochondrion; clathrin-coated pit; coated vesicle; extracellular exosome; extracellular matrix; mitochondrial matrix; extracellular space; mitochondrial inner membrane; cytosol; plasma membrane; cell surface; membrane; secretory granule; protein-containing complex;
Biological process	chaperone-mediated protein complex assembly; positive regulation of interleukin-12 production; positive regulation of interleukin-10 production; protein stabilization; protein maturation; positive regulation of macrophage activation; MyD88-dependent toll-like receptor signaling pathway; isotype switching to IgG isotypes; B cell activation; B cell cytokine production; response to unfolded protein; B cell proliferation; protein folding; positive regulation of T cell mediated immune response to tumor cell; protein refolding; positive regulation of interleukin-6 production; positive regulation of apoptotic process; response to cold; viral process; activation of cysteine-type endopeptidase activity involved in apoptotic process; regulation of transcription by RNA polymerase II; 'de novo' protein folding; protein import into mitochondrial intermembrane space; chaperone-mediated protein folding; apoptotic mitochondrial changes; positive regulation of interferon-alpha production; positive regulation of interferon-gamma production; T cell activation; negative regulation of apoptotic process; positive regulation of T cell activation; mitochondrion organization;
	Sources:Amigo / QuickGO
Orthologs
	3329
	15510
	ENSG00000144381
	ENSMUSG00000025980
	P10809
	P63038
	NM_002156; NM_199440
	NM_010477; NM_001356512
	NP_002147; NP_955472
	NP_034607; NP_001343441
	Wikidata
View/Edit Human	View/Edit Mouse

GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria. It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES. In eukaryotes the organellar proteins Hsp60 and Hsp10 are structurally and functionally nearly identical to GroEL and GroES, respectively, due to their endosymbiotic origin.

HSP60 is implicated in mitochondrial protein import and macromolecular assembly. It may facilitate the correct folding of imported proteins, and may also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. HSP60 interacts with HRAS and with HBV protein X and HTLV-1 protein p40tax. HSP60 belongs to the chaperonin (HSP60) family. Note: This description may include information from UniProtKB.

Alternate Names: 60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HSP-60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HSPD1

Heat shock protein 60 (HSP60) is a mitochondrial chaperonin that is typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains into their respective three-dimensional structure. Through the extensive study of groEL, HSP60’s bacterial homolog, HSP60 has been deemed essential in the synthesis and transportation of essential mitochondrial proteins from the cell's cytoplasm into the mitochondrial matrix. Further studies have linked HSP60 to diabetes, stress response, cancer and certain types of immunological disorders.

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